Reviewed, UniProtKB/Swiss-Prot Q6G4D7 (PDXH_BARHE)

Names and origin

Protein names

Recommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidase
    EC=1.4.3.5
Alternative name(s):
    PNP/PMP oxidase
      Short name=PNPOx
    Pyridoxal 5'-phosphate synthase

Gene names

Name:	pdxH
Ordered Locus Names:	BH04290

Organism

Bartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]

Taxonomic identifier

38323 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629 Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: HAMAP pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167684
Regions
	Nucleotide binding	68 – 69	2	FMN By similarity
	Nucleotide binding	132 – 133	2	FMN By similarity
	Region	183 – 185	3	Substrate binding By similarity
Sites
	Binding site	53	1	FMN By similarity
	Binding site	56	1	FMN; via amide nitrogen By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	75	1	FMN By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	123	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G4D7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 7702729BA8E64A47	FASTA	207	24,271
	10 20 30 40 50 60 MGNTVQTDND FMQMQKPFAL FAKWLEEATV SEINDPNAMA LATVDKTGFP NVRMVLLKDF 70 80 90 100 110 120 SPQGFVFYTN YESPKGQEIL KSMKASLVFH WKSLRRQVRI RGIVEKVTPQ EADAYFQSRP 130 140 150 160 170 180 RDSRIGAWAS KQSQPLESRF VLEKAIARYT TRYAVGNIPR PPYWSGFRVK PLSIEFWCDR 190 200 PFRLHDRLLF TRDSVEHVDW KRQKLYP

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX897699 Genomic DNA. Translation: CAF27238.1.
RefSeq	YP_033267.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2865013.
GenomeReviews	Gene locus BH04290 in contig BX897699_GR.
KEGG	bhe:BH04290.
NMPDR	fig|283166.1.peg.395.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6G4D7.
OMA	Q6G4D7. EPFALFA.
Enzyme and pathway databases
BioCyc	BHEN283166:BH04290-MON.
BRENDA	1.4.3.5. 277357.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR011576. PNPOx_rel_FMN_bd_core. IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN_bd. [Graphical view]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHER	PTHR10851. Pyridox_oxidase. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
ProDom	PD006312. Pyridox_oxidase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_BARHE

Accession

Primary (citable) accession number: Q6G4D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)